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Protein

Molybdopterin molybdenumtransferase

Gene

moeA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.1 Publication

Catalytic activityi

Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • molybdenum incorporation into molybdenum-molybdopterin complex Source: EcoCyc
  • Mo-molybdopterin cofactor biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciEcoCyc:EG10153-MONOMER.
ECOL316407:JW0811-MONOMER.
MetaCyc:EG10153-MONOMER.
RETL1328306-WGS:GSTH-2187-MONOMER.
BRENDAi2.10.1.1. 2026.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin molybdenumtransferase (EC:2.10.1.1)
Short name:
MPT Mo-transferase
Gene namesi
Name:moeA
Synonyms:bisB, chlE, narE
Ordered Locus Names:b0827, JW0811
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10153. moeA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Molybdopterin molybdenumtransferasePRO_0000170989Add
BLAST

Proteomic databases

EPDiP12281.
PaxDbiP12281.
PRIDEiP12281.

Interactioni

Subunit structurei

Homodimer. Interacts with MobA, MogA and MobB in vivo.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mobAP321733EBI-554393,EBI-1133881

Protein-protein interaction databases

BioGridi4259979. 8 interactions.
DIPiDIP-10240N.
IntActiP12281. 8 interactions.
MINTiMINT-1250871.
STRINGi511145.b0827.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2011Combined sources
Beta strandi27 – 315Combined sources
Helixi32 – 343Combined sources
Beta strandi39 – 424Combined sources
Beta strandi50 – 534Combined sources
Beta strandi55 – 639Combined sources
Helixi65 – 706Combined sources
Beta strandi76 – 816Combined sources
Beta strandi82 – 843Combined sources
Beta strandi95 – 984Combined sources
Beta strandi110 – 1134Combined sources
Helixi114 – 1163Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi123 – 1264Combined sources
Turni132 – 1354Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi147 – 1504Combined sources
Turni158 – 1603Combined sources
Helixi161 – 1666Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi179 – 1857Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi192 – 1943Combined sources
Helixi205 – 21511Combined sources
Beta strandi219 – 2268Combined sources
Helixi230 – 24314Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi255 – 2573Combined sources
Helixi260 – 2689Combined sources
Beta strandi269 – 28012Combined sources
Beta strandi283 – 2886Combined sources
Beta strandi290 – 2967Combined sources
Helixi301 – 31010Combined sources
Helixi312 – 3209Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi331 – 3377Combined sources
Beta strandi345 – 35511Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi361 – 3655Combined sources
Helixi376 – 3794Combined sources
Beta strandi381 – 3866Combined sources
Beta strandi398 – 4036Combined sources
Helixi406 – 4083Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FC5X-ray2.20A/B1-411[»]
1G8LX-ray1.95A/B1-411[»]
1G8RX-ray2.65A/B1-411[»]
2NQKX-ray2.90A/B1-411[»]
2NQMX-ray3.00A/B1-411[»]
2NQNX-ray2.20A/B1-411[»]
2NQQX-ray2.40A/B/C/D1-411[»]
2NQRX-ray2.20A/B1-411[»]
2NQSX-ray2.50A/B1-411[»]
2NQUX-ray2.70A/B1-411[»]
2NQVX-ray2.82A/B1-411[»]
2NROX-ray2.50A/B1-411[»]
2NRPX-ray3.00A/B1-411[»]
2NRSX-ray2.80A/B1-411[»]
ProteinModelPortaliP12281.
SMRiP12281. Positions 5-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12281.

Family & Domainsi

Sequence similaritiesi

Belongs to the MoeA family.Curated

Phylogenomic databases

eggNOGiENOG4105CVM. Bacteria.
COG0303. LUCA.
HOGENOMiHOG000280652.
InParanoidiP12281.
KOiK03750.
OMAiCMLESHT.
OrthoDBiEOG66MQMC.
PhylomeDBiP12281.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 1 hit.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 1 hit.
PROSITEiPS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFTTGLMSL DTALNEMLSR VTPLTAQETL PLVQCFGRIL ASDVVSPLDV
60 70 80 90 100
PGFDNSAMDG YAVRLADIAS GQPLPVAGKS FAGQPYHGEW PAGTCIRIMT
110 120 130 140 150
GAPVPEGCEA VVMQEQTEQM DNGVRFTAEV RSGQNIRRRG EDISAGAVVF
160 170 180 190 200
PAGTRLTTAE LPVIASLGIA EVPVIRKVRV ALFSTGDELQ LPGQPLGDGQ
210 220 230 240 250
IYDTNRLAVH LMLEQLGCEV INLGIIRDDP HALRAAFIEA DSQADVVISS
260 270 280 290 300
GGVSVGEADY TKTILEELGE IAFWKLAIKP GKPFAFGKLS NSWFCGLPGN
310 320 330 340 350
PVSATLTFYQ LVQPLLAKLS GNTASGLPAR QRVRTASRLK KTPGRLDFQR
360 370 380 390 400
GVLQRNADGE LEVTTTGHQG SHIFSSFSLG NCFIVLERDR GNVEVGEWVE
410
VEPFNALFGG L
Length:411
Mass (Da):44,067
Last modified:October 1, 1989 - v1
Checksum:i6DBBC2B4191F5951
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21151 Genomic DNA. Translation: AAA23579.1.
U00096 Genomic DNA. Translation: AAC73914.1.
AP009048 Genomic DNA. Translation: BAA35515.1.
PIRiA32352.
RefSeqiNP_415348.1. NC_000913.3.
WP_000397340.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73914; AAC73914; b0827.
BAA35515; BAA35515; BAA35515.
GeneIDi945454.
KEGGiecj:JW0811.
eco:b0827.
PATRICi32116857. VBIEscCol129921_0854.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21151 Genomic DNA. Translation: AAA23579.1.
U00096 Genomic DNA. Translation: AAC73914.1.
AP009048 Genomic DNA. Translation: BAA35515.1.
PIRiA32352.
RefSeqiNP_415348.1. NC_000913.3.
WP_000397340.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FC5X-ray2.20A/B1-411[»]
1G8LX-ray1.95A/B1-411[»]
1G8RX-ray2.65A/B1-411[»]
2NQKX-ray2.90A/B1-411[»]
2NQMX-ray3.00A/B1-411[»]
2NQNX-ray2.20A/B1-411[»]
2NQQX-ray2.40A/B/C/D1-411[»]
2NQRX-ray2.20A/B1-411[»]
2NQSX-ray2.50A/B1-411[»]
2NQUX-ray2.70A/B1-411[»]
2NQVX-ray2.82A/B1-411[»]
2NROX-ray2.50A/B1-411[»]
2NRPX-ray3.00A/B1-411[»]
2NRSX-ray2.80A/B1-411[»]
ProteinModelPortaliP12281.
SMRiP12281. Positions 5-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259979. 8 interactions.
DIPiDIP-10240N.
IntActiP12281. 8 interactions.
MINTiMINT-1250871.
STRINGi511145.b0827.

Proteomic databases

EPDiP12281.
PaxDbiP12281.
PRIDEiP12281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73914; AAC73914; b0827.
BAA35515; BAA35515; BAA35515.
GeneIDi945454.
KEGGiecj:JW0811.
eco:b0827.
PATRICi32116857. VBIEscCol129921_0854.

Organism-specific databases

EchoBASEiEB0151.
EcoGeneiEG10153. moeA.

Phylogenomic databases

eggNOGiENOG4105CVM. Bacteria.
COG0303. LUCA.
HOGENOMiHOG000280652.
InParanoidiP12281.
KOiK03750.
OMAiCMLESHT.
OrthoDBiEOG66MQMC.
PhylomeDBiP12281.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG10153-MONOMER.
ECOL316407:JW0811-MONOMER.
MetaCyc:EG10153-MONOMER.
RETL1328306-WGS:GSTH-2187-MONOMER.
BRENDAi2.10.1.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP12281.
PROiP12281.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 1 hit.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 1 hit.
PROSITEiPS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis."
    Nohno T., Kasai Y., Saito T.
    J. Bacteriol. 170:4097-4102(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli."
    Hasona A., Ray R.M., Shanmugam K.T.
    J. Bacteriol. 180:1466-1472(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli."
    Magalon A., Frixon C., Pommier J., Giordano G., Blasco F.
    J. Biol. Chem. 277:48199-48204(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOBA; MOGA AND MOBB.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "In vitro molybdenum ligation to molybdopterin using purified components."
    Nichols J.D., Rajagopalan K.V.
    J. Biol. Chem. 280:7817-7822(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS MPT--MO LIGASE.
  8. "The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway."
    Schrag J.D., Huang W., Sivaraman J., Smith C., Plamondon J., Larocque R., Matte A., Cygler M.
    J. Mol. Biol. 310:419-431(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, SUBUNIT, COFACTOR.
  9. "The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin."
    Xiang S., Nichols J., Rajagopalan K.V., Schindelin H.
    Structure 9:299-310(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiMOEA_ECOLI
AccessioniPrimary (citable) accession number: P12281
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: March 16, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.